serval:BIB_E1EF6AEE1CB4
Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats.
10.1098/rsob.170078
000404841600008
28659383
Rafie
K.
author
Raimi
O.
author
Ferenbach
A.T.
author
Borodkin
V.S.
author
Kapuria
V.
author
van Aalten
DMF
author
article
2017-06
Open biology
2046-2441
2046-2441
journal
7
6
170078
O-linked <i>N</i> -acetylglucosamine (O-GlcNAc) is an essential and dynamic post-translational modification found on hundreds of nucleocytoplasmic proteins in metazoa. Although a single enzyme, O-GlcNAc transferase (OGT), generates the entire cytosolic O-GlcNAc proteome, it is not understood how it recognizes its protein substrates, targeting only a fraction of serines/threonines in the metazoan proteome for glycosylation. We describe a trapped complex of human OGT with the C-terminal domain of TAB1, a key innate immunity-signalling O-GlcNAc protein, revealing extensive interactions with the tetratricopeptide repeats of OGT. Confirmed by mutagenesis, this interaction suggests that glycosylation substrate specificity is achieved by recognition of a degenerate sequon in the active site combined with an extended conformation C-terminal of the O-GlcNAc target site.
Adaptor Proteins, Signal Transducing/drug effects
Adaptor Proteins, Signal Transducing/genetics
Amino Acid Sequence
Glycosylation
Humans
N-Acetylglucosaminyltransferases/genetics
N-Acetylglucosaminyltransferases/metabolism
Sequence Alignment
Substrate Specificity
Tetratricopeptide Repeat/genetics
Tetratricopeptide Repeat/physiology
O-GlcNAc
O-GlcNAc transferase
glycosylation
signalling
substrate recognition
eng
60_published
true
peer-reviewed
Publication types: Journal Article
Publication Status: ppublish
University of Lausanne
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